CHED 802 |
| Rhizza Renfro, Brad Thuro, and Jacqueline Bennett. The Walter H. Hoffman Department of Chemistry, Drury University, 900 N. Benton, Springfield, MO 65802 |
| Peptides are often analyzed by HPLC following fluorescent derivatization of amino groups by such reagents as OPA and FMOC-Cl. We are trying to make fluorescent coumarin derivatives of tyrosine-containing peptides. Although tyrosine is abundant in biomolecules, its chemical reactivity in aqueous solution is extremely low making it difficult to selectively modify except when present in an enzyme's active site. Currently, we are studying coumarin formation in phenols by the Pechmann condensation with ethyl acetoacetate under a variety of conditions. The reactions being studied now are performed in ionic liquid with various Lewis or Bronsted acid catalysts, such as Amberlyst-15 or L-proline. The ionic liquid [bmim]BF4 is used as a solvent due to its solubility properties and environmental friendliness. Ionic liquids have low volatility, are outstandingly good solvents for a wide range of both inorganic and organic materials, and have the potential for reuse. We have had some limited success with p-substituted phenols and much greater success with the more widely studied m-substituted phenols. If we succeed, this procedure would provide an alternative for detection of tyrosine-containing peptides. There is some evidence to support coumarin adducts of tyrosine residues in proteins, a possible cause of some long-term pathologies in diabetes. According to the Centers for Disease Control, more than 17 million Americans have diabetes, and over 200,000 people die each year of related complications. |
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Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Poster
Division of Chemical Education |